Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.4.3 (phospholipase C)
 18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lipid-acyl hydrolases (LAHases) play significant roles in lipid degradation during the storage of vegetables. In particular, spinach contains a large portion of galactolipids (59.5%) and phospholipids (22.4%) among its fat-soluble components, which are used as substrates for LAHases. Thermal inactivation of various LAHases, including phospholipases A, C, and D, phosphatase, and galactolipase, from spinach and carrot was investigated to optimize the blanching process prior to the frozen storage of vegetables. Thermostability of phospholipase C or galactolipase was greatest among the LAHases from both spinach and carrot. Galactolipase from spinach exhibited a D value of 3.39 x 10(2) s at 80 degrees C and a z value of 8.21 degrees C, whereas phospholipase C from spinach showed D(80) of 1.72 x 10(2) s with a z value of 9.26 degrees C. In the case of LAHases from carrot, the D(65) and z values of galactolipase were 6.66 x 10(2) s and 8.69 degrees C, respectively, whereas phospholipase C displayed D(85) of 3.12 x 10(2) s and a z value of 15.8 degrees C. Highly active and thermostable galactolipase and phospholipase C in spinach and carrot made it possible for them to be used as indicator enzymes for the determination of quality deterioration of the stored vegetables.
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PMID:Thermal inactivation kinetics and application of phospho- and galactolipid-degrading enzymes for evaluation of quality changes in frozen vegetables. 1136 83

The role of acyl lipids in the in vitro stabilization of the oligomeric form of light-harvesting complex II of winter rye (Secale cereale L. cv Muskateer) grown at 5 or 20 degrees C was investigated. Purified light-harvesting complex II was enzymically delipidated to various extents by treatment with the following lipolytic enzymes: phospholipase C, phospholipase A(2), and galactolipase. Complete removal of phosphatidylcholine had no effect on the stability of the oligomeric form, whereas the removal of phosphatidylcholine plus phosphatidylglycerol caused a decrease in the ratio of oligomeric:monomeric forms from 1.86 +/- 0.17 to 0.85 +/- 0.17 and 3.51 +/- 0.82 to 0.81 +/- 0.29 for purified cold-hardened and nonhardened light-harvesting complex II, respectively, with no change in free pigment content. Incubation of delipidated cold-hardened or nonhardened light-harvesting complex with purified thylakoid phosphatidylglycerol containing trans-Delta(3)-hexadecenoic acid resulted in 48% reconstitution of the oligomeric form on a total chlorophyll basis with an oligomer:monomer of about 1.90. Incubation in the presence of di- 16:0 or di- 18:1 phosphatidylglycerol, phosphatidylcholine, monogalactosyldiacylglyceride, or digalactosyldiacylglyceride caused no oligomerization, but rather a further destabilization of the monomeric form. These lipid-dependent structural changes were correlated with significant changes in the 77K fluorescence emission spectra for purified light-harvesting complex II. We conclude that the stabilization of the supramolecular organization of light-harvesting complex II from rye is specifically dependent upon molecular species of phosphatidylglycerol containing trans-Delta(3)-hexadecenoic acid.
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PMID:The Role of Acyl Lipids in Reconstitution of Lipid-Depleted Light-Harvesting Complex II from Cold-Hardened and Nonhardened Rye. 1665 78